SEPA_STAES
ID SEPA_STAES Reviewed; 507 AA.
AC P0C0Q4; P43148;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Extracellular elastase;
DE EC=3.4.24.-;
DE AltName: Full=SEPP1;
DE Flags: Precursor;
GN Name=sepA; OrderedLocusNames=SE_2219;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
CC -!- FUNCTION: Protease that has a low substrate specificity. Glucagon is
CC preferentially cleaved between aromatic (Phe) and hydrophobic (Val)
CC amino acids. Hydrolyzes casein and elastin (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR EMBL; AE015929; AAO05861.1; -; Genomic_DNA.
DR RefSeq; NP_765774.1; NC_004461.1.
DR RefSeq; WP_002456744.1; NZ_WBME01000025.1.
DR AlphaFoldDB; P0C0Q4; -.
DR SMR; P0C0Q4; -.
DR STRING; 176280.SE_2219; -.
DR MEROPS; M04.009; -.
DR EnsemblBacteria; AAO05861; AAO05861; SE_2219.
DR GeneID; 50017712; -.
DR KEGG; sep:SE_2219; -.
DR PATRIC; fig|176280.10.peg.2166; -.
DR eggNOG; COG3227; Bacteria.
DR HOGENOM; CLU_008590_5_2_9; -.
DR OMA; WKHIKLT; -.
DR Proteomes; UP000001411; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.390.10; -; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR025711; PepSY.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF03413; PepSY; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Calcium; Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted;
KW Signal; Zinc; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..207
FT /evidence="ECO:0000250"
FT /id="PRO_0000042923"
FT CHAIN 208..507
FT /note="Extracellular elastase"
FT /id="PRO_0000042924"
FT ACT_SITE 352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 435
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 507 AA; 55787 MW; 055BB5344351EF22 CRC64;
MKNFSKFALT SIAALTVASP LVNTEVDAKD KVSATQNIDA KVTQESQATN ALKELPKSEN
IKKHYKDYKV TDTEKDNKGF THYTLQPKVG NTYAPDKEVK VHTNKEGKVV LVNGDTDAKK
VQPTNKVAIS KESATDKAFE AIKIDRQKAK NLKSDVIKTN KVEIDGEKNK YVYNIEIITT
SPKISHWNVK IDAETGQVVD KLNMIKEAAT TGTGKGVLGD TKQININSVS GGYALQDLTQ
QGTLSAYNYD ANTGQAYLMQ DKDKNFVDDE QRAGVDANYY AKETYDYYKN TFGRESYDNQ
GSPIISIAHV NNFQGQDNRN NAAWIGDKMI YGDGDGRTFT ALSGANDVVA HEITHGVTQQ
TANLVYRSQS GALNESFSDV FGYFIDDEDF LMGEDVYTPG VGGDALRSMS NPERFGQPSH
MNDFVYTNSD NGGVHTNSGI PNKAAYNTIR SIGKQRSEQI YYRALTVYLT SNSDFQDAKA
SLQQAAFDLY GDGIAQQVGQ AWDSVGV
